Structural biology

Part of a series on
Biochemistry
Chemistry of life
Index Outline History
Key components Biomolecules Enzymes Gene expression Metabolism
List of biochemists Biochemist List of biochemists
Biomolecule families Carbohydrates: Alcohols Glycoproteins Glycosides Lipids: Eicosanoids Fatty acids Fatty-acid metabolism Glycerides Phospholipids Sphingolipids Cholesterol Steroids Nucleic acids: Nucleobases Nucleosides Nucleotides Nucleotide metabolism Proteins: Amino acids Amino acid metabolism Other: Tetrapyrroles Heme
Chemical synthesis Artificial gene synthesis Biomimetic synthesis Bioretrosynthesis Biosynthesis Chemosynthesis Convergent synthesis Custom peptide synthesis Direct process Divergent synthesis Electrosynthesis Enantioselective synthesis Fully automated synthesis Hydrothermal synthesis LASiS Mechanosynthesis One-pot synthesis Organic synthesis Peptide synthesis Radiosynthesis Retrosynthesis Semisynthesis Solid-phase synthesis Solvothermal synthesis Total synthesis Volume combustion synthesis
Biochemistry fields Molecular biology Cell biology Chemical biology Bioorthogonal chemistry Medicinal chemistry Pharmacology Clinical chemistry Neurochemistry Bioorganic chemistry Bioorganometallic chemistry Bioinorganic chemistry Biophysical chemistry Bacteriology parasitology virology immunology
Glossaries Glossary of biology Glossary of chemistry
Category
v t e

Structural biology, as defined by the Journal of Structural Biology, deals with structural analysis of living material (formed, composed of, and/or maintained and refined by living cells) at every level of organization. Early structural biologists throughout the 19th and early 20th centuries were primarily only able to study structures to the limit of the naked eye's visual acuity and through magnifying glasses and light microscopes.

In the 20th century, a variety of experimental techniques were developed to examine the 3D structures of biological molecules. The most prominent techniques are X-ray crystallography, nuclear magnetic resonance, and electron microscopy. Through the discovery of X-rays and its applications to protein crystals, structural biology was revolutionized, as now scientists could obtain the three-dimensional structures of biological molecules in atomic detail.^[1] Likewise, NMR spectroscopy allowed information about protein structure and dynamics to be obtained.^[2] Finally, in the 21st century, electron microscopy also saw a drastic revolution with the development of more coherent electron sources, aberration correction for electron microscopes, and reconstruction software that enabled the successful implementation of high resolution cryo-electron microscopy, thereby permitting the study of individual proteins and molecular complexes in three-dimensions at angstrom resolution.

With the development of these three techniques, the field of structural biology expanded and also became a branch of molecular biology, biochemistry, and biophysics concerned with the molecular structure of biological macromolecules (especially proteins, made up of amino acids, RNA or DNA, made up of nucleotides, and membranes, made up of lipids), how they acquire the structures they have, and how alterations in their structures affect their function.^[3] This subject is of great interest to biologists because macromolecules carry out most of the functions of cells, and it is only by coiling into specific three-dimensional shapes that they are able to perform these functions. This architecture, the "tertiary structure" of molecules, depends in a complicated way on each molecule's basic composition, or "primary structure." At lower resolutions, tools such as FIB-SEM tomography have allowed for greater understanding of cells and their organelles in 3-dimensions, and how each hierarchical level of various extracellular matrices contributes to function (for example in bone). In the past few years it has also become possible to predict highly accurate physical molecular models to complement the experimental study of biological structures.^[4] Computational techniques such as molecular dynamics simulations can be used in conjunction with empirical structure determination strategies to extend and study protein structure, conformation and function.^[5]